ID   CAPSD_BPPHK             Reviewed;         431 AA.
AC   Q38041;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Capsid protein F;
DE   AltName: Full=F protein;
DE   AltName: Full=GPF;
GN   Name=F;
OS   Enterobacteria phage phiK (Bacteriophage phi-K).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Bullavirinae; Alphatrevirus.
OX   NCBI_TaxID=10848;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (PHI-K AND MUTANT PHI KHT).
RX   PubMed=8827438; DOI=10.1093/oxfordjournals.jbchem.a021348;
RA   Kodaira K., Oki M., Kakikawa M., Kimoto H., Taketo A.;
RT   "The virion proteins encoded by bacteriophage phi K and its host-range
RT   mutant phi KhT: host-range determination and DNA binding properties.";
RL   J. Biochem. 119:1062-1069(1996).
CC   -!- FUNCTION: Assembles to form an icosahedral capsid with a T=1 symmetry,
CC       about 30 nm in diameter, and consisting of 60 capsid proteins F. Upon
CC       virus binding to host cell, one of the spikes dissociates from the
CC       capsid and the virus interacts with LPS through the exposed EF loops on
CC       the F proteins. After the genome had been ejected, the channel formed
CC       by the F proteins at the unique fivefold axis remains open.
CC       {ECO:0000250|UniProtKB:P03641}.
CC   -!- SUBUNIT: Pentamerizes and interacts with H protein, G and B pentamers
CC       to form 12S pre-assembly complex. By binding with protein D, induces
CC       joining of twelve 12S complex to form the procapsid. The procapsid has
CC       an external scaffold made of 240 copies of protein D, 60 copies of the
CC       internally located B protein, and contains 60 copies of each of the
CC       viral structural proteins F and G. Upon genome packaging, interacts
CC       with protein J. The mature virion is composed of 60 copies each of the
CC       F, G, and J proteins, and 12 copies of the H protein.
CC       {ECO:0000250|UniProtKB:P03641}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03641}.
CC   -!- MISCELLANEOUS: Phi KhT, a host-range mutant of phi K, can grow on
CC       E.coli C and B, besides K12, and is more thermosensitive than the
CC       parental phage phi K.
CC   -!- SIMILARITY: Belongs to the microviridae F protein family.
CC       {ECO:0000305}.
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DR   EMBL; X60323; CAA42891.1; -; Genomic_DNA.
DR   PIR; JC4805; JC4805.
DR   RefSeq; NP_043949.1; NC_001730.1.
DR   SMR; Q38041; -.
DR   GeneID; 1261199; -.
DR   KEGG; vg:1261199; -.
DR   Proteomes; UP000002122; Genome.
DR   GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.169.10; -; 1.
DR   InterPro; IPR016184; Capsid/spike_ssDNA_virus.
DR   InterPro; IPR003514; Microviridae_protein_F.
DR   InterPro; IPR037002; Microviridae_protein_F_sf.
DR   Pfam; PF02305; Phage_F; 2.
DR   SUPFAM; SSF88645; SSF88645; 1.
PE   3: Inferred from homology;
KW   Capsid protein; T=1 icosahedral capsid protein;
KW   Viral genome ejection through host cell envelope;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03641"
FT   CHAIN           2..431
FT                   /note="Capsid protein F"
FT                   /id="PRO_0000164889"
SQ   SEQUENCE   431 AA;  49239 MW;  907226BFF8AC2AC0 CRC64;
     MSNVQTSAER EIVDLSHLAF DCGMIGRLKT VSWTPVIAGD SFELDAVGAL RLSPLRRGLA
     IDSKVDFFTF YIPHRHVYGD QWIQFMRDGV DASPLPSVTT TKYPDDAGYV GTIVPKSNRI
     PKFLHQSYLN IYNNYFRAPW MPERTEANPS NLDRDDSRYG FRCCHLKTIW SAPLPPETKL
     AEQMGIESNS IDIMGLQAAY AQLHTEQERT YFMQRYRDVI SSFGGSTSYD ADNRPLLVMH
     TDFWASGYDV DGTDQSSLGQ FSGRVQQTFK HSVPRFFVPE HGVMMTLMLV RFPPISPLEH
     HYLVGRNNLT YTDLAGDPAL IGNLPPREIS YQDLFRDGRP GIKIKVAESI WYRTHPDYVN
     YKYQLLEGFP FLDDAPGTTS GDDLQKAILI DHNDYNACFQ SQQLLQWNNQ ARYNVNVYRH
     IPTVRDSIMT S